Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Secreted effector protein PipB2

Gene

pipB2

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Involved in the reorganization of late endosome/lysosome (LE/Lys) compartments in mammalian cells. Necessary and sufficient to link kinesin-1 onto the Salmonella-containing vacuole (SCV) membrane. Required for centrifugal extension of lysosomal glycoprotein-rich membrane tubules, known as Salmonella-induced filaments (Sifs), away from the SCV and toward the cell periphery. Required for virulence, but not for intracellular survival and replication in phagocytic cells.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2796-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted effector protein PipB2
Alternative name(s):
Type III effector PipB2
Gene namesi
Name:pipB2
Ordered Locus Names:STM2780
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Secreted
  • Host membrane

  • Note: Secreted via the type III secretion system 2 (SPI-2 TTSS), and delivered into the host cell. In phagocytic cells localizes to the Salmonella-containing vacuole (SCV) and tubular extensions from the SCV, Salmonella-induced filaments (Sifs). In epithelial cells localizes to peripheral vesicles, in addition to SCVs and Sifs. Concentrates in detergent-resistant microdomains (DRMs), present on the intracellular membranes of SCVs and Sifs.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi340 – 3401T → A: No effect. 1 Publication
Mutagenesisi341 – 3411L → A: Prevents the peripheral accumulation of GFP-PipB2 and LAMP-1. Slightly affects its LE/Lys redistribution. 1 Publication
Mutagenesisi342 – 3421F → A: Partial reduction in the peripheral accumulation of GFP-PipB2 and LAMP-1. 1 Publication
Mutagenesisi343 – 3431N → A: Increases LAMP-1 redistribution. No effect on peripheral accumulation of GFP-PipB2. 1 Publication
Mutagenesisi344 – 3441E → A: Decreases LAMP-1 redistribution. No effect on peripheral accumulation of GFP-PipB2. 1 Publication
Mutagenesisi345 – 3451F → A: Prevents LE/Lys redistribution. Does not affect the peripheral accumulation of GFP-PipB2. 1 Publication
Mutagenesisi346 – 3461Y → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Secreted effector protein PipB2PRO_0000278299Add
BLAST

Proteomic databases

PaxDbiQ8ZMM8.
PRIDEiQ8ZMM8.

Expressioni

Inductioni

Expression of the gene is regulated by the two-component regulatory system SsrA/SsrB. It is also activated by SlyA and controlled by the two-component regulatory system PhoP/PhoQ.

Interactioni

Subunit structurei

Interacts with the host kinesin light chain (KLC), a subunit of the kinesin-1 motor complex.1 Publication

Protein-protein interaction databases

DIPiDIP-61260N.
STRINGi99287.STM2780.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 255Combined sources
Helixi30 – 4314Combined sources
Beta strandi47 – 493Combined sources
Helixi50 – 6819Combined sources
Beta strandi69 – 746Combined sources
Beta strandi78 – 858Combined sources
Beta strandi88 – 936Combined sources
Beta strandi103 – 1108Combined sources
Beta strandi113 – 1208Combined sources
Helixi121 – 13515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LEZNMR-A17-161[»]
ProteinModelPortaliQ8ZMM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini162 – 20140Pentapeptide repeat 1Add
BLAST
Domaini202 – 24140Pentapeptide repeat 2Add
BLAST
Domaini247 – 28640Pentapeptide repeat 3Add
BLAST
Domaini287 – 32640Pentapeptide repeat 4Add
BLAST

Domaini

Contains various tandem pentapeptide repeats in the C-terminal region. The pentapeptide motif is required to efficiently recruit kinesin-1. No position is completely conserved in these repeats, whose consensus sequence is A-[DN]-[FLM]-X-X. The C-terminal 38 amino acids residues, specifically, the C-terminal motif LFNEF, are required for peripheral localization of PipB2 and redistribution of lysosomal-associated membrane protein (LAMP). The N-terminal 225 amino acids residues are sufficient for type III translocation and association with Sifs and SCVs, but not accumulation in peripheral vesicles.1 Publication

Sequence similaritiesi

Contains 4 pentapeptide repeat domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105VRE. Bacteria.
COG1357. LUCA.
HOGENOMiHOG000028269.
KOiK15352.
OMAiFNVFYSE.
PhylomeDBiQ8ZMM8.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
[Graphical view]
PfamiPF00805. Pentapeptide. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8ZMM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSLDSLAG MAKSAFGAGT SAAMRQATSP KTILEYIINF FTCGGIRRRN
60 70 80 90 100
ETQYQELIET MAETLKSTMP DRGAPLPENI ILDDMDGCRV EFNLPGENNE
110 120 130 140 150
AGQVIVRVSK GDHSETREIP LASFEKICRA LLFRCEFSLP QDSVILTAQG
160 170 180 190 200
GMNLKGAVLT GANLTSENLC DADLSGANLE GAVLFMADCE GANFKGANLS
210 220 230 240 250
GTSLGDSNFK NACLEDSIMC GATLDHANLT GANLQHASLL GCSMIECNCS
260 270 280 290 300
GANMDHTNLS GATLIRADMS GATLQGATIM AAIMEGAVLT RANLRKASFI
310 320 330 340 350
STNLDGADLA EANLNNTCFK DCTLTDLRTE DATMSTSTQT LFNEFYSENI
Length:350
Mass (Da):37,274
Last modified:March 1, 2002 - v1
Checksum:i701D5EFBA7EB11EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY532917 Genomic DNA. Translation: AAS66036.1.
AE006468 Genomic DNA. Translation: AAL21665.1.
RefSeqiNP_461706.1. NC_003197.1.
WP_001738474.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21665; AAL21665; STM2780.
GeneIDi1254303.
KEGGistm:STM2780.
PATRICi32384228. VBISalEnt20916_2931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY532917 Genomic DNA. Translation: AAS66036.1.
AE006468 Genomic DNA. Translation: AAL21665.1.
RefSeqiNP_461706.1. NC_003197.1.
WP_001738474.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LEZNMR-A17-161[»]
ProteinModelPortaliQ8ZMM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61260N.
STRINGi99287.STM2780.

Proteomic databases

PaxDbiQ8ZMM8.
PRIDEiQ8ZMM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21665; AAL21665; STM2780.
GeneIDi1254303.
KEGGistm:STM2780.
PATRICi32384228. VBISalEnt20916_2931.

Phylogenomic databases

eggNOGiENOG4105VRE. Bacteria.
COG1357. LUCA.
HOGENOMiHOG000028269.
KOiK15352.
OMAiFNVFYSE.
PhylomeDBiQ8ZMM8.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2796-MONOMER.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
[Graphical view]
PfamiPF00805. Pentapeptide. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIPB2_SALTY
AccessioniPrimary (citable) accession number: Q8ZMM8
Secondary accession number(s): Q6QNB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2002
Last modified: September 7, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.